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- W2075653889 abstract "Abstract The molecular recognition of a novel kind of hybrid conjugates, composed of artificial biomimetic β‐peptide oligomers with an O ‐linked natural N ‐acetyl‐galactosamine (the Tn‐antigen) residue, by four different GalNAc specific lectins was investigated using surface plasmon biosensor technology. The influence of the peptide and the glycosyl moiety on the recognition was studied using two glycosylated β 3 ‐heptapeptides, a glycosylated α‐heptapeptide, two β‐amino acid containing dipeptides, and monomeric αGalNAc‐ O ‐Thr. Although all four lectins displayed a decreased affinity for the carbohydrate residue when attached to a peptide, as compared to the monomeric Tn‐antigen, the peptide part was found to have distinct effects on the binding kinetics—indicating that varying degrees of protein–peptide interactions occurred in the recognition process. Likewise, the lectins did not discriminate between β 3 ‐peptides and the α‐peptide, but the β‐linkage of the galactose had a detrimental effect for at least two of the lectins. Copyright © 2007 John Wiley & Sons, Ltd." @default.
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- W2075653889 date "2007-03-01" @default.
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- W2075653889 title "Biomolecular recognition of glycosylated β3-peptides by GalNAc specific lectins" @default.
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- W2075653889 doi "https://doi.org/10.1002/jmr.821" @default.
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